The domain within your query sequence starts at position 24 and ends at position 110; the E-value for the Resistin domain shown below is 2.7e-39.

PLCPIDEAIDKKIKQDFNSLFPNAIKNIGLNCWTVSSRGKLASCPEGTAVLSCSCGSACG
SWDIREEKVCHCQCARIDWTAARCCKL

Resistin

Resistin
PFAM accession number:PF06954
Interpro abstract (IPR009714):

RELMs, secreted proteins with roles including insulin resistance and the activation of inflammatory processes, are also known as found in inflammatory zone (FIZZ), and include four members in mouse (RELM-alpha/FIZZ1/HIMF, RELM-beta/FIZZ2, Resistin/FIZZ3, and RELM-gamma/FIZZ4) and two members in human (resistin and RELM-beta). RELMs are potentially implicated in a wide range of physiological and pathological processes including obesity-associated diabetes, cardiovascular system function, cancer development and metastasis [ (PUBMED:11201732) (PUBMED:24320036) (PUBMED:28192887) (PUBMED:29866514) ].

There are significant differences between human and rodent RELMs with respect to gene and protein structure, differential gene regulation, different tissue distribution profiles, and insulin resistance induction. Resistin appears to convey insulin resistance in rodents, and to instigate inflammatory processes in humans. In the pathophysiology of obesity-associated diabetes, mouse resistin is secreted by adipocytes and increases hepatic gluconeogenesis, thereby promoting insulin resistance, human resistin is secreted by macrophages and may play a role through inflammatory contributions [ (PUBMED:12594039) (PUBMED:26662574) ].

Elevated levels of human resistin have been reported in various cancers including colorectal, endometrial, and postmenopausal breast cancers, and may initiate the production of further inflammatory cytokines, to promote tumor cell progression [ (PUBMED:27001185) ]. Resistin has also been shown to cause G1 arrest in colon cancer cells. However, resistin may interfere with chemotherapy [ (PUBMED:28417458) ].

Resistin contains an N-terminal signal sequence, a variable middle section, and a conserved C-terminal domain. The C-terminal domain is comprised of a cysteine signature motif sequence shared by all RELM family members, which is proposed to be critical for disulfide bond formation and protein folding [ (PUBMED:29866514) ]. Resistin circulates as hexamers and trimers; structural similarity has been noted between the resistin homotrimer and the proprotein convertase subtilisin/kexin type 9, C-terminal cysteine-rich domain [ (PUBMED:15155948) (PUBMED:18975914) ].

GO component:extracellular region (GO:0005576)
GO function:hormone activity (GO:0005179)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Resistin